Abstract
We report the first high-resolution structural data for the β/γ-peptide 13-helix (i,i+3 CO⋯HN H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of β- and γ-amino acid residues. Our characterization includes both crystallophaphic and 2D NMR data. Previous studies suggested that β/γ-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized β- and γ-residues, which strongly promote 13-helical folding by the 1:1 β/γ backbone.
| Original language | English |
|---|---|
| Pages (from-to) | 7868-7869 |
| Number of pages | 2 |
| Journal | Journal of the American Chemical Society |
| Volume | 132 |
| Issue number | 23 |
| DOIs | |
| Publication status | Published - 2010 Jun 16 |
All Science Journal Classification (ASJC) codes
- Catalysis
- Chemistry(all)
- Biochemistry
- Colloid and Surface Chemistry
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Guo, L., Almeida, A. M., Zhang, W., Reidenbach, A. G., Choi, S. H., Guzei, I. A., & Gellman, S. H. (2010). Helix formation in preorganized β/γ-peptide foldamers: Hydrogen-bond analogy to the α-helix without α-amino acid residues. Journal of the American Chemical Society, 132(23), 7868-7869. https://doi.org/10.1021/ja103233a